USP9X hydrolyzes Ub:PEX5S yielding PEX5S and Ubiquitin

Stable Identifier
R-HSA-9033478
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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The deubiquitinating enzyme USP9X hydrolyzes the thioester bond between the carboxyl terminus of ubiquitin and cysteine-11 of PEX5S (inferred from the large isoform of PEX5L in Grou et al. 2012). The thioester bond is unstable and appears also to be spontaneously disrupted by nucleophilic attack of small metabolites such as reduced glutathione (Grou et al. 2009).

Literature References
PubMed ID Title Journal Year
22371489 Identification of ubiquitin-specific protease 9X (USP9X) as a deubiquitinase acting on ubiquitin-peroxin 5 (PEX5) thioester conjugate

Grou, CP, Francisco, T, Rodrigues, TA, Freitas, MO, Pinto, MP, Carvalho, AF, Domingues, P, Wood, SA, Rodríguez-Borges, JE, Sá-Miranda, C, Fransen, M, Azevedo, JE

J. Biol. Chem. 2012
19208625 Properties of the ubiquitin-pex5p thiol ester conjugate

Grou, CP, Carvalho, AF, Pinto, MP, Huybrechts, SJ, Sá-Miranda, C, Fransen, M, Azevedo, JE

J. Biol. Chem. 2009
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
thiol-dependent ubiquitinyl hydrolase activity of USP9X:Ub:PEX5S [cytosol]
Physical Entity
Activity
Inferred From
Authored
Reviewed
Created